1dec
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(New page: 200px<br /><applet load="1dec" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dec" /> '''STRUCTURE OF THE RGD PROTEIN DECORSIN: CONSE...)
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Revision as of 11:05, 20 November 2007
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STRUCTURE OF THE RGD PROTEIN DECORSIN: CONSERVED MOTIF AND DISTINCT FUNCTION IN LEECH PROTEINS THAT AFFECT BLOOD CLOTTING
Overview
The structure of the leech protein decorsin, a potent 39-residue, antagonist of glycoprotein IIb-IIIa and inhibitor of platelet aggregation, was determined by nuclear magnetic resonance. In contrast to other, disintegrins, the Arg-Gly-Asp (RGD)-containing region of decorsin is well, defined. The three-dimensional structure of decorsin is similar to that of, hirudin, an anticoagulant leech protein that potently inhibits thrombin., Amino acid sequence comparisons suggest that ornatin, another glycoprotein, IIb-IIIa antagonist, and antistasin, a potent Factor Xa inhibitor and, anticoagulant found in leeches, share the same structural motif. Although, decorsin, hirudin, and antistasin all affect the blood clotting process, and appear similar in structure, their mechanisms of action and epitopes, important for binding to their respective targets are distinct.
About this Structure
1DEC is a Single protein structure of sequence from Macrobdella decora. Full crystallographic information is available from OCA.
Reference
Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting., Krezel AM, Wagner G, Seymour-Ulmer J, Lazarus RA, Science. 1994 Jun 24;264(5167):1944-7. PMID:8009227
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